ID A0A0L9TEY3_PHAAN Unreviewed; 928 AA.
AC A0A0L9TEY3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=LR48_Vigan627s003100 {ECO:0000313|EMBL:KOM28982.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM28982.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001250,
CC ECO:0000256|RuleBase:RU362083};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC ECO:0000256|RuleBase:RU362083}.
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DR EMBL; KQ258464; KOM28982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9TEY3; -.
DR STRING; 3914.A0A0L9TEY3; -.
DR EnsemblPlants; KOM28982; KOM28982; LR48_Vigan627s003100.
DR Gramene; KOM28982; KOM28982; LR48_Vigan627s003100.
DR OMA; EVKGIGW; -.
DR Proteomes; UP000053144; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 6.10.140.890; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR42861:SF124; ATPASE 3, PLASMA MEMBRANE-TYPE-RELATED; 1.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW Ion transport {ECO:0000256|RuleBase:RU362083};
KW Magnesium {ECO:0000256|RuleBase:RU362083};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362083};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362083};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT TRANSMEM 67..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 102..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 220..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 258..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 626..648
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 654..671
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 691..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 732..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 763..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 796..813
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 19..91
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 928 AA; 102386 MW; E17AC5A9438CC847 CRC64;
MAADKAAITL DQIKNETVDL ERIPIEEVFQ QLKCSREGLS SEEGASRLQI FGPNKLEEKK
ESKLLKFLGF MWNPLSWVME AAAIMAIALA NGDGRPPDWQ DFVGIVCLLV INSTISFIEE
NNAGNAAAAL MAGLAPKTKV LRDGKWTEQE AAILVPGDII SIKLESLPAT KGPGDEVFSG
STCKQGEIEA VVIATGVHTF FGKAAHLVDS TNQVGHFQKV LTAIGNFCIC SIAVGMLAEI
IVMYPIQHRK YRDGIDNLLV LLIGGIPIAM PTVLSVTMAI GSHRLSQQGA ITKRMTAIEE
MAGMDVLCSD KTGTLTLNKL SVDKNLIEVF AKGVDKDHVI LLAARASRTE NQDAIDAAIV
GMLADPKEAR AGVREVHFLP FNPVDKRTAL TYIDADGNWH RASKGAPEQI MTLCNLREDA
KKKVHSIIDK FAERGLRSLA VARQEVPEKT KESAGSPWQF VGLLSLFDPP RHDSAETIRR
ALHLGVNVKM ITGDQLAIAK ETGRRLGMGT NMYPSASLLG QDKDASIAAL PVEELIEKAD
GFAGVFPEHK YEIVKKLQDR KHICGMTGDG VNDAPALKKA DIGIAVADAT DAARSASDIV
LTEPGLSVII SAVLTSRAIF QRMKNYTIYA VSITIRIVFG FMFIALIWKF DFSPFMVLII
AILNDGTIMT ISKDRVKPSP LPDSWKLQEI FATGVVLGSY LALMTIIFFW AMEQTNFFPE
KFGVRHLTHD EMMSALYLQV SIVSQALIFV TRSRSWSFVE RPGMLLVIAF VIAQLIATII
AVYADWSFAK VKGIGWGWAG VIWLYSIVFY FPLDLMKFAI RYILSGKAWL NLLENKTAFT
TKKDYGKEER EAQWAHAQRT LHGLQPPETT SIFNEKNSYR ELSEIAEQAR KRAEVARLRE
LHTLKGHVES VVKLKGLDID TIQQHYTV
//
